Correlation between Hemichrome Stability and the Root Effect in Tetrameric Hemoglobins

Autor: Vergara, Alessandro, Franzese, Marisa, Merlino, Antonello, Bonomi, Giovanna, Verde, Cinzia, Giordano, Daniela, di Prisco, Guido, Lee, H. Caroline, Peisach, Jack, Mazzarella, Lelio

Publikováno v: In Biophysical Journal 5 August 2009 97(3):866-874

The Role of the Hinge Loop in Domain Swapping: THE SPECIAL CASE OF BOVINE SEMINAL RIBONUCLEASE

Autor: Picone, Delia ^‡, Di Fiore, Anna ^‡, Ercole, Carmine ^‡, Franzese, Marisa ^‡, Sica, Filomena ^{‡, §}, Tomaselli, Simona ^‡, Mazzarella, Lelio ^{‡, §, ¶}

Publikováno v: In Journal of Biological Chemistry 8 April 2005 280(14):13771-13778

Correlation between Root effect and hemichrome stability in tetrameric hemoglobins

Autor: VERGARA, ALESSANDRO, FRANZESE, MARISA, MERLINO, ANTONELLO, BONOMI, GIOVANNA, MAZZARELLA, LELIO, C. Verde, D. Giordano, G. Di Prisco, C. Lee, J. Peisach

Publikováno v: Biophysical journal
97 (2009): 866–874.
info:cnr-pdr/source/autori:A. Vergara, M. Franzese, A. Merlino, G. Bonomi, C. Verde, D. Giordano, G. Di Prisco, C. Lee, J. Peisach, L. Mazzarella/titolo:Correlation between Root effect and hemichrome stability in tetrameric hemoglobins/doi:/rivista:Biophysical journal (Print)/anno:2009/pagina_da:866/pagina_a:874/intervallo_pagine:866–874/volume:97

Oxidation of Hbs leads to the formation of different forms of Fe(III) that are relevant to a range of biochemical and physiological functions. Here we report a combined EPR/x-ray crystallography study performed at acidic pH on six ferric tetrameric H

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::aade0122a3dedd1506d4c00361d61dce
http://www.cnr.it/prodotto/i/14107

Linkage between Root effect and hemichrome stability

Autor: Alessandro Vergara, Antonello Merlino, Franzese, Marisa, Di Prisco, G., Verde, C., Peisach, J., Lee, C., Mazzarella, Lelio

Publikováno v: Università degli Studi di Napoli Federico II
VII European Symposium of the. Protein Society, Stoccolma, 2007
info:cnr-pdr/source/autori:A.Vergara, A. Merlino, M. Franzese, G. Di Prisco, C. Verde, J. Peisach, C. Lee, L. Mazzarella/congresso_nome:VII European Symposium of the. Protein Society/congresso_luogo:Stoccolma/congresso_data:2007/anno:2007/pagina_da:/pagina_a:/intervallo_pagine

Antarctic fish hemoglobins (AFHbs) exhibit a peculiar oxidation process. Upon oxidation, these tetrameric proteins show a remarkable propensity to evolve toward the formation of hemichrome, a species in which both proximal and distal hystidines are b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::324f486fa38682e6647b037e733bd15c
http://hdl.handle.net/11588/307836

Stereochemistry, formation and reactivity of hemichromes in Antarctic fish hemoglobins

Autor: Alessandro Vergara, Antonello Merlino, Franzese, Marisa, Di Prisco, G., Verde, C., Peisach, J., Lee, C., Mazzarella, Lelio

Publikováno v: XIVth International Conference on Dioxygen binding and sensing proteins, Napoli, 2006
info:cnr-pdr/source/autori:A.Vergara, A. Merlino, M. Franzese, G. Di Prisco, C. Verde, J. Peisach, C. Lee, L. Mazzarella/congresso_nome:XIVth International Conference on Dioxygen binding and sensing proteins/congresso_luogo:Napoli/congresso_data:2006/anno:2006/pagina_da:/pagina_a:/intervallo_pagine
Università degli Studi di Napoli Federico II

Antarctic fish hemoglobins (AF-Hbs) exhibit an unusual auto-oxidation process. Our previous crystallographic and spectroscopic investigations have demonstrated that, upon oxidation, these tetrameric proteins show a remarkable propensity to evolve tow

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::3684618625f9bb256b47314ec450003c
http://hdl.handle.net/11588/307834